Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P31040 (SDHA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit of complex II
Short name=Fp
Gene names
Name:SDHA
Synonyms:SDH2, SDHF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor. Ref.12

Catalytic activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

FAD.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.

Subunit structure

Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD. Interacts with SDHAF2/SDH5; interaction is required for FAD attachment. Interacts with TRAP1. Ref.10 Ref.15

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.

Post-translational modification

Phosphorylation at Tyr-215 is important for efficient electron transfer in complex II and the prevention of ROS generation.

Deacetylated by SIRT3 By similarity.

Involvement in disease

Mitochondrial complex II deficiency (MT-C2D) [MIM:252011]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations. Clinical features include psychomotor regression in infants, poor growth with lack of speech development, severe spastic quadriplegia, dystonia, progressive leukoencephalopathy, muscle weakness, exercise intolerance, cardiomyopathy. Some patients manifest Leigh syndrome or Kearns-Sayre syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.8

Cardiomyopathy, dilated 1GG (CMD1GG) [MIM:613642]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

Paragangliomas 5 (PGL5) [MIM:614165]: A neural crest tumor usually derived from the chromoreceptor tissue of a paraganglion. Paragangliomas can develop at various body sites, including the head, neck, thorax and abdomen. Most commonly, they are located in the head and neck region, specifically at the carotid bifurcation, the jugular foramen, the vagal nerve, and in the middle ear.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Sequence caution

The sequence CAA37886.1 differs from that shown. Reason: Differs extensively from that shown.

Ontologies

Keywords
   Biological processElectron transport
Transport
Tricarboxylic acid cycle
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DiseaseCardiomyopathy
Disease mutation
Leigh syndrome
Tumor suppressor
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular metabolic process

Traceable author statement. Source: Reactome

nervous system development

Inferred from mutant phenotype PubMed 16361598. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay Ref.8. Source: UniProtKB

respiratory electron transport chain

Inferred from direct assay Ref.8. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

succinate metabolic process

Inferred from direct assay Ref.8. Source: UniProtKB

tricarboxylic acid cycle

Traceable author statement Ref.8. Source: UniProtKB

   Cellular_componentmitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial respiratory chain complex II

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 16826196Ref.8. Source: UniProtKB

   Molecular_functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

succinate dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SDHBP219122EBI-1057265,EBI-1056481

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion By similarity
Chain44 – 664621Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
PRO_0000010335

Regions

Nucleotide binding68 – 736FAD By similarity
Nucleotide binding91 – 10616FAD By similarity
Nucleotide binding456 – 4572FAD By similarity

Sites

Active site3401Proton acceptor By similarity
Binding site2751FAD By similarity
Binding site2961Substrate By similarity
Binding site3081Substrate By similarity
Binding site4071Substrate By similarity
Binding site4401FAD By similarity
Binding site4511Substrate By similarity

Amino acid modifications

Modified residue991Tele-8alpha-FAD histidine By similarity
Modified residue1671N6-acetyllysine By similarity
Modified residue1791N6-acetyllysine; alternate Ref.11
Modified residue1791N6-succinyllysine; alternate By similarity
Modified residue1821N6-acetyllysine By similarity
Modified residue2151Phosphotyrosine; by SRC Ref.14
Modified residue2501N6-acetyllysine; alternate By similarity
Modified residue2501N6-succinyllysine; alternate By similarity
Modified residue3351N6-acetyllysine; alternate Ref.11
Modified residue3351N6-succinyllysine; alternate By similarity
Modified residue4801N6-acetyllysine By similarity
Modified residue4851N6-acetyllysine; alternate By similarity
Modified residue4851N6-succinyllysine; alternate By similarity
Modified residue4981N6-acetyllysine; alternate By similarity
Modified residue4981N6-succinyllysine; alternate By similarity
Modified residue5171N6-acetyllysine By similarity
Modified residue5381N6-acetyllysine; alternate By similarity
Modified residue5381N6-succinyllysine; alternate By similarity
Modified residue5411N6-acetyllysine Ref.11
Modified residue5471N6-acetyllysine; alternate By similarity
Modified residue5471N6-succinyllysine; alternate By similarity
Modified residue5501N6-acetyllysine By similarity
Modified residue5981N6-acetyllysine By similarity
Modified residue6081N6-acetyllysine Ref.11
Modified residue6151N6-succinyllysine By similarity
Modified residue6241N6-acetyllysine By similarity
Modified residue6361N6-acetyllysine By similarity
Modified residue6471N6-acetyllysine By similarity

Natural variations

Natural variant331F → V.
Corresponds to variant rs1061518 [ dbSNP | Ensembl ].
VAR_049214
Natural variant381D → V.
Corresponds to variant rs34635677 [ dbSNP | Ensembl ].
VAR_049215
Natural variant2401E → Q.
Corresponds to variant rs1041946 [ dbSNP | Ensembl ].
VAR_049216
Natural variant3331V → I.
Corresponds to variant rs1062468 [ dbSNP | Ensembl ].
VAR_059307
Natural variant5241A → V in LS. Ref.3
VAR_016878
Natural variant5541R → W in LS. Ref.8
VAR_002449
Natural variant5551G → E in MT-C2D and CMD1GG. Ref.16 Ref.17
VAR_016879
Natural variant5891R → W in PGL5; loss of activity. Ref.12
VAR_065975
Natural variant6571V → I. Ref.2
Corresponds to variant rs6962 [ dbSNP | Ensembl ].
VAR_049217

Experimental info

Sequence conflict3561G → D in AAD51006. Ref.3
Sequence conflict3981E → D in AAD51006. Ref.3
Sequence conflict5911A → T in AAD51006. Ref.3
Sequence conflict5961D → G in AAD51006. Ref.3
Sequence conflict6001R → Q in AAD51006. Ref.3
Sequence conflict6291Y → F in AAA20683. Ref.2
Sequence conflict6401E → G in AAD51006. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P31040 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 180B664E3FFD0B34

FASTA66472,692
        10         20         30         40         50         60 
MSGVRGLSRL LSARRLALAK AWPTVLQTGT RGFHFTVDGN KRASAKVSDS ISAQYPVVDH 

        70         80         90        100        110        120 
EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR 

       130        140        150        160        170        180 
WHFYDTVKGS DWLGDQDAIH YMTEQAPAAV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF 

       190        200        210        220        230        240 
GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE 

       250        260        270        280        290        300 
DGSIHRIRAK NTVVATGGYG RTYFSCTSAH TSTGDGTAMI TRAGLPCQDL EFVQFHPTGI 

       310        320        330        340        350        360 
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE 

       370        380        390        400        410        420 
KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ 

       430        440        450        460        470        480 
VLRHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IEESCRPGDK 

       490        500        510        520        530        540 
VPPIKPNAGE ESVMNLDKLR FADGSIRTSE LRLSMQKSMQ NHAAVFRVGS VLQEGCGKIS 

       550        560        570        580        590        600 
KLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR 

       610        620        630        640        650        660 
IDEYDYSKPI QGQQKKPFEE HWRKHTLSYV DVGTGKVTLE YRPVIDKTLN EADCATVPPA 


IRSY 

« Hide

References

« Hide 'large scale' references
[1]"Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the flavoprotein (Fp) subunit of liver mitochondria."
Hirawake H., Wang H., Kuramochi T., Kojima S., Kita K.
J. Biochem. 116:221-227(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"The cDNA sequence of the flavoprotein subunit of human heart succinate dehydrogenase."
Morris A.A.M., Farnsworth L., Ackrell B.A.C., Turnbull D.M., Birch-MacHin M.A.
Biochim. Biophys. Acta 1185:125-128(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-657.
Tissue: Heart.
[3]"Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome."
Parfait B., Chretien D., Roetig A., Marsac C., Munnich A., Rustin P.
Hum. Genet. 106:236-243(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LS VAL-524.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[7]"Cloning of the flavoprotein subunit of human succinate dehydrogenase."
Malcovati M., Marchetti L., Zanelli E., Tenchini M.L.
(In) Curti B., Ronchi S., Zanetti G. (eds.); Flavins and flavoproteins 1990, pp.727-730, Walter de Gruyter, Berlin (1991)
Cited for: PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[8]"Mutation of a nuclear succinate dehydrogenase gene results in mitochondrial respiratory chain deficiency."
Bourgeron T., Rustin P., Chretien D., Birch-MacHin M.A., Bourgeois M., Viegas-Pequignot E., Munnich A., Roetig A.
Nat. Genet. 11:144-149(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 546-562, VARIANT LS TRP-554.
[9]"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 76-92 AND 398-418.
Tissue: Adipocyte.
[10]"SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma."
Hao H.-X., Khalimonchuk O., Schraders M., Dephoure N., Bayley J.-P., Kunst H., Devilee P., Cremers C.W.R.J., Schiffman J.D., Bentz B.G., Gygi S.P., Winge D.R., Kremer H., Rutter J.
Science 325:1139-1142(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SDHAF2.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-335; LYS-541 AND LYS-608, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"SDHA is a tumor suppressor gene causing paraganglioma."
Burnichon N., Briere J.J., Libe R., Vescovo L., Riviere J., Tissier F., Jouanno E., Jeunemaitre X., Benit P., Tzagoloff A., Rustin P., Bertherat J., Favier J., Gimenez-Roqueplo A.P.
Hum. Mol. Genet. 19:3011-3020(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANT PGL5 TRP-589, CHARACTERIZATION OF VARIANT PGL5 TRP-589.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Mitochondrial c-Src regulates cell survival through phosphorylation of respiratory chain components."
Ogura M., Yamaki J., Homma M.K., Homma Y.
Biochem. J. 447:281-289(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-215.
[15]"The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase."
Sciacovelli M., Guzzo G., Morello V., Frezza C., Zheng L., Nannini N., Calabrese F., Laudiero G., Esposito F., Landriscina M., Defilippi P., Bernardi P., Rasola A.
Cell Metab. 17:988-999(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAP1.
[16]"Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II."
Van Coster R., Seneca S., Smet J., Van Hecke R., Gerlo E., Devreese B., Van Beeumen J., Leroy J.G., De Meirleir L., Lissens W.
Am. J. Med. Genet. A 120:13-18(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MT-C2D GLU-555.
[17]"Familial neonatal isolated cardiomyopathy caused by a mutation in the flavoprotein subunit of succinate dehydrogenase."
Levitas A., Muhammad E., Harel G., Saada A., Caspi V.C., Manor E., Beck J.C., Sheffield V., Parvari R.
Eur. J. Hum. Genet. 18:1160-1165(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1GG GLU-555.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30648 mRNA. Translation: BAA06332.1.
L21936 mRNA. Translation: AAA20683.1.
AF171030 expand/collapse EMBL AC list , AF171017, AF171018, AF171019, AF171020, AF171021, AF171022, AF171023, AF171024, AF171025, AF171026, AF171027, AF171028, AF171029 Genomic DNA. Translation: AAD51006.1.
AK291311 mRNA. Translation: BAF84000.1.
CH471235 Genomic DNA. Translation: EAW50983.1.
BC001380 mRNA. Translation: AAH01380.1.
X53943 mRNA. Translation: CAA37886.1. Sequence problems.
S79641 Genomic DNA. Translation: AAB35332.1.
PIRJX0336.
S21302.
RefSeqNP_004159.2. NM_004168.2.
UniGeneHs.440475.

3D structure databases

ProteinModelPortalP31040.
SMRP31040. Positions 52-664.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112290. 63 interactions.
IntActP31040. 15 interactions.
MINTMINT-3012212.
STRING9606.ENSP00000264932.

Chemistry

ChEMBLCHEMBL5758.
DrugBankDB00139. Succinic acid.

PTM databases

PhosphoSiteP31040.

Polymorphism databases

DMDM1169337.

2D gel databases

REPRODUCTION-2DPAGEIPI00305166.

Proteomic databases

PaxDbP31040.
PeptideAtlasP31040.
PRIDEP31040.

Protocols and materials databases

DNASU6389.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264932; ENSP00000264932; ENSG00000073578.
GeneID6389.
KEGGhsa:6389.
UCSCuc003jao.4. human.

Organism-specific databases

CTD6389.
GeneCardsGC05P000208.
H-InvDBHIX0120996.
HGNCHGNC:10680. SDHA.
HPACAB034929.
HPA041981.
MIM252011. phenotype.
256000. phenotype.
600857. gene.
613642. phenotype.
614165. phenotype.
neXtProtNX_P31040.
Orphanet154. Familial isolated dilated cardiomyopathy.
44890. Gastrointestinal stromal tumor.
29072. Hereditary pheochromocytoma-paraganglioma.
3208. Isolated succinate-CoQ reductase deficiency.
255241. Leigh syndrome with leukodystrophy.
PharmGKBPA35605.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1053.
HOVERGENHBG001461.
InParanoidP31040.
KOK00234.
OMAINVFGKR.
OrthoDBEOG7MH0XJ.
PhylomeDBP31040.
TreeFamTF300763.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000073578-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00223; UER01006.

Gene expression databases

ArrayExpressP31040.
BgeeP31040.
CleanExHS_SDHA.
GenevestigatorP31040.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSDHA.
GenomeRNAi6389.
NextBio24820.
PROP31040.
SOURCESearch...

Entry information

Entry nameSDHA_HUMAN
AccessionPrimary (citable) accession number: P31040
Secondary accession number(s): A8K5J6, Q16395, Q9UMY5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM